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Conserved domains on  [gi|157817207|ref|NP_001101679|]
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serine protease 40 precursor [Rattus norvegicus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
71-313 2.99e-79

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 242.95  E-value: 2.99e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  71 IYGGQIAGAQRWPWQASLRLY-GRHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTRYSRKMSVKKLIVH 149
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 150 KDYNKFyPQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVrlPLPNDLYEAELIIMSNDDCK 229
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 230 GFFPPPvpgssktYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLEGSWYVVGLTSWSSSCEDPiSSPSVFARVSYFDKW 309
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                 ....
gi 157817207 310 ISDN 313
Cdd:cd00190  229 IQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
71-313 2.99e-79

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 242.95  E-value: 2.99e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  71 IYGGQIAGAQRWPWQASLRLY-GRHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTRYSRKMSVKKLIVH 149
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 150 KDYNKFyPQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVrlPLPNDLYEAELIIMSNDDCK 229
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 230 GFFPPPvpgssktYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLEGSWYVVGLTSWSSSCEDPiSSPSVFARVSYFDKW 309
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                 ....
gi 157817207 310 ISDN 313
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
70-310 1.28e-74

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 231.03  E-value: 1.28e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207    70 KIYGGQIAGAQRWPWQASLRLYG-RHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTrYSRKMSVKKLIV 148
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   149 HKDYNKfYPQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVRlPLPNDLYEAELIIMSNDDC 228
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   229 KGFFPPPvpgssktYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLeGSWYVVGLTSWSSSCEDPiSSPSVFARVSYFDK 308
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 157817207   309 WI 310
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
71-310 9.38e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 176.86  E-value: 9.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   71 IYGGQIAGAQRWPWQASLRLY-GRHICGAVLIDKNWVASAAHCFqmsRNPGDYQIMLGYTKLNSPTRYSRKMSVKKLIVH 149
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  150 KDYNKFYpQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVRlplPNDLYEAELIIMSNDDCK 229
Cdd:pfam00089  78 PNYNPDT-LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  230 GFFPPpvpgssktyYIYDDMVCAADYSltKSICSGDSGGPLVCLLEgswYVVGLTSWSSSCEDPiSSPSVFARVSYFDKW 309
Cdd:pfam00089 154 SAYGG---------TVTDTMICAGAGG--KDACQGDSGGPLVCSDG---ELIGIVSWGYGCASG-NYPGVYTPVSSYLDW 218

                  .
gi 157817207  310 I 310
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
68-312 1.59e-49

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.52  E-value: 1.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  68 QGKIYGGQIAGAQRWPWQASLRL---YGRHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTRYSRKmsVK 144
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLSTSGGTVVK--VA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 145 KLIVHKDYNKFYPqGSDIVLLQLHSSVEYSShilPACVPNKNITIPKEKACWTSGWGNLREDVRlPLPNDLYEAELIIMS 224
Cdd:COG5640  105 RIVVHPDYDPATP-GNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 225 NDDCKGFfpppvpgsskTYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLEGSWYVVGLTSWSSS-CEDpiSSPSVFARV 303
Cdd:COG5640  180 DATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA--GYPGVYTRV 247

                 ....*....
gi 157817207 304 SYFDKWISD 312
Cdd:COG5640  248 SAYRDWIKS 256
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
71-313 2.99e-79

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 242.95  E-value: 2.99e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  71 IYGGQIAGAQRWPWQASLRLY-GRHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTRYSRKMSVKKLIVH 149
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 150 KDYNKFyPQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVrlPLPNDLYEAELIIMSNDDCK 229
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 230 GFFPPPvpgssktYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLEGSWYVVGLTSWSSSCEDPiSSPSVFARVSYFDKW 309
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                 ....
gi 157817207 310 ISDN 313
Cdd:cd00190  229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
70-310 1.28e-74

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 231.03  E-value: 1.28e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207    70 KIYGGQIAGAQRWPWQASLRLYG-RHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTrYSRKMSVKKLIV 148
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   149 HKDYNKfYPQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVRlPLPNDLYEAELIIMSNDDC 228
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   229 KGFFPPPvpgssktYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLeGSWYVVGLTSWSSSCEDPiSSPSVFARVSYFDK 308
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 157817207   309 WI 310
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
71-310 9.38e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 176.86  E-value: 9.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   71 IYGGQIAGAQRWPWQASLRLY-GRHICGAVLIDKNWVASAAHCFqmsRNPGDYQIMLGYTKLNSPTRYSRKMSVKKLIVH 149
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  150 KDYNKFYpQGSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSGWGNLREDVRlplPNDLYEAELIIMSNDDCK 229
Cdd:pfam00089  78 PNYNPDT-LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  230 GFFPPpvpgssktyYIYDDMVCAADYSltKSICSGDSGGPLVCLLEgswYVVGLTSWSSSCEDPiSSPSVFARVSYFDKW 309
Cdd:pfam00089 154 SAYGG---------TVTDTMICAGAGG--KDACQGDSGGPLVCSDG---ELIGIVSWGYGCASG-NYPGVYTPVSSYLDW 218

                  .
gi 157817207  310 I 310
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
68-312 1.59e-49

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.52  E-value: 1.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207  68 QGKIYGGQIAGAQRWPWQASLRL---YGRHICGAVLIDKNWVASAAHCFQmSRNPGDYQIMLGYTKLNSPTRYSRKmsVK 144
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLSTSGGTVVK--VA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 145 KLIVHKDYNKFYPqGSDIVLLQLHSSVEYSShilPACVPNKNITIPKEKACWTSGWGNLREDVRlPLPNDLYEAELIIMS 224
Cdd:COG5640  105 RIVVHPDYDPATP-GNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207 225 NDDCKGFfpppvpgsskTYYIYDDMVCAADYSLTKSICSGDSGGPLVCLLEGSWYVVGLTSWSSS-CEDpiSSPSVFARV 303
Cdd:COG5640  180 DATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA--GYPGVYTRV 247

                 ....*....
gi 157817207 304 SYFDKWISD 312
Cdd:COG5640  248 SAYRDWIKS 256
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
82-199 6.67e-08

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 50.62  E-value: 6.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817207   82 WPWQASLRLYGRHICGAVLIDKNWVASAAHCFQMSRNPGDY-QIMLGYTKlnsptrysRKMSVK---KLIVHKDYNKFYP 157
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAK--------TLKSIEgpyEQIVRVDCRHDIP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 157817207  158 QgSDIVLLQLHSSVEYSSHILPACVPNKNITIPKEKACWTSG 199
Cdd:pfam09342  73 E-SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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